Summary: Lipopolysaccharide kinase (Kdo/WaaP) family
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Lipopolysaccharide kinase (Kdo/WaaP) family Edit Wikipedia article
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The family consists of lipopolysaccharide kinases including lipopolysaccharide core heptose(I) kinase rfaP (encoded by the waaP (rfaP) gene). Lipopolysaccharide core heptose(I) kinase rfaP is required for the addition of phosphate to O-4 of the first heptose residue of the lipopolysaccharide (LPS) inner core region. It has previously been shown that it is necessary for resistance to hydrophobic and polycationic antimicrobials in E. coli and that it is required for virulence in invasive strains of Salmonella enterica. The family also includes 3-deoxy-D-manno-octulosonic acid kinase (KDO kinase) from Haemophilus influenzae, which phosphorylates Kdo-lipid IV(A), a lipopolysaccharide precursor, and is involved in virulence.
- Yethon JA, Whitfield C (February 2001). "Purification and characterization of WaaP from Escherichia coli, a lipopolysaccharide kinase essential for outer membrane stability". J. Biol. Chem. 276 (8): 5498–504. doi:10.1074/jbc.M008255200. PMID 11069912.
- White KA, Lin S, Cotter RJ, Raetz CR (1999). "A Haemophilus influenzae gene that encodes a membrane bound 3-deoxy-D-manno-octulosonic acid (Kdo) kinase. Possible involvement of kdo phosphorylation in bacterial virulence.". J Biol Chem 274 (44): 31391–400. PMID 10531340.
- Krupa A, Srinivasan N (2002). "Lipopolysaccharide phosphorylating enzymes encoded in the genomes of Gram-negative bacteria are related to the eukaryotic protein kinases.". Protein Sci 11 (6): 1580–4. doi:10.1110/ps.3560102. PMC 2373617. PMID 12021457.
Lipopolysaccharide kinase (Kdo/WaaP) family Provide feedback
These lipopolysaccharide kinases are related to protein kinases PF00069. This family includes waaP (rfaP) gene product is required for the addition of phosphate to O-4 of the first heptose residue of the lipopolysaccharide (LPS) inner core region. It has previously been shown that WaaP is necessary for resistance to hydrophobic and polycationic antimicrobials in E. coli and that it is required for virulence in invasive strains of S. enterica .
Yethon JA, Whitfield C; , J Biol Chem 2001;276:5498-5504.: Purification and characterization of WaaP from Escherichia coli, a lipopolysaccharide kinase essential for outer membrane stability. PUBMED:11069912 EPMC:11069912
Krupa A, Srinivasan N; , Protein Sci 2002;11:1580-1584.: Lipopolysaccharide phosphorylating enzymes encoded in the genomes of Gram-negative bacteria are related to the eukaryotic protein kinases. PUBMED:12021457 EPMC:12021457
White KA, Lin S, Cotter RJ, Raetz CR; , J Biol Chem 1999;274:31391-31400.: A Haemophilus influenzae gene that encodes a membrane bound 3-deoxy-D-manno-octulosonic acid (Kdo) kinase. Possible involvement of kdo phosphorylation in bacterial virulence. PUBMED:10531340 EPMC:10531340
External database links
This tab holds annotation information from the InterPro database.
InterPro entry IPR010440
Protein phosphorylation, which plays a key role in most cellular activities, is a reversible process mediated by protein kinases and phosphoprotein phosphatases. Protein kinases catalyse the transfer of the gamma phosphate from nucleotide triphosphates (often ATP) to one or more amino acid residues in a protein substrate side chain, resulting in a conformational change affecting protein function. Phosphoprotein phosphatases catalyse the reverse process. Protein kinases fall into three broad classes, characterised with respect to substrate specificity [PUBMED:3291115]:
- Serine/threonine-protein kinases
- Tyrosine-protein kinases
- Dual specificity protein kinases (e.g. MEK - phosphorylates both Thr and Tyr on target proteins)
Protein kinase function is evolutionarily conserved from Escherichia coli to human [PUBMED:12471243]. Protein kinases play a role in a multitude of cellular processes, including division, proliferation, apoptosis, and differentiation [PUBMED:12368087]. Phosphorylation usually results in a functional change of the target protein by changing enzyme activity, cellular location, or association with other proteins. The catalytic subunits of protein kinases are highly conserved, and several structures have been solved [PUBMED:15078142], leading to large screens to develop kinase-specific inhibitors for the treatments of a number of diseases [PUBMED:15320712].
This entry represents lipopolysaccharide kinases which are related to protein kinases INTERPRO. This family includes waaP (rfaP) gene product is required for the addition of phosphate to O-4 of the first heptose residue of the lipopolysaccharide (LPS) inner core region. It has previously been shown that WaaP is necessary for resistance to hydrophobic and polycationic antimicrobials in E. coli and that it is required for virulence in invasive strains of Salmonella enterica [PUBMED:11069912].
|Cellular component||membrane (GO:0016020)|
|Molecular function||ATP binding (GO:0005524)|
|phosphotransferase activity, alcohol group as acceptor (GO:0016773)|
|Biological process||lipopolysaccharide biosynthetic process (GO:0009103)|
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This superfamily includes the Serine/Threonine- and Tyrosine- protein kinases as well as related kinases that act on non-protein substrates.
The clan contains the following 19 members:ABC1 APH APH_6_hur Choline_kinase DUF1679 DUF2252 EcKinase Fructosamin_kin Kdo Kinase-like PIP49_C Pkinase Pkinase_Tyr Pox_ser-thr_kin RIO1 Seadorna_VP7 UL97 WaaY YrbL-PhoP_reg
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Curation and family details
|Seed source:||Krupa A, Srinivasan N|
|Number in seed:||14|
|Number in full:||2201|
|Average length of the domain:||187.20 aa|
|Average identity of full alignment:||22 %|
|Average coverage of the sequence by the domain:||64.55 %|
|HMM build commands:||
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||9|
|Download:||download the raw HMM for this family|
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